1,6-anhydro-N-acetylmuramic acid | 104430-66-2

• 分子结构分类: 有机化合物 - 有机杂环化合物 - 氧杂环己烷
• 英文名称: 1,6-anhydro-N-acetylmuramic acid
• 英文别名: 2-(2-Acetylamino-4-hydroxy-6,8-dioxa-bicyclo[3.2.1]oct-3-yloxy)-propionic acid；(2R)-2-[[(1R,2S,3R,4R,5R)-4-acetamido-2-hydroxy-6,8-dioxabicyclo[3.2.1]octan-3-yl]oxy]propanoic acid
• CAS: 104430-66-2
• 化学式: C₁₁H₁₇NO₇
• 分子量: 275.258
• InChiKey: ZFEGYUMHFZOYIY-YVNCZSHWSA-N

物化性质

• 沸点：
  624.7±55.0 °C(Predicted)
• 密度：
  1.43±0.1 g/cm3(Predicted)

计算性质

• 辛醇/水分配系数(LogP)：
  -1.6
• 重原子数：
  19
• 可旋转键数：
  4
• 环数：
  2.0
• sp3杂化的碳原子比例：
  0.82
• 拓扑面积：
  114
• 氢给体数：
  3
• 氢受体数：
  7

反应信息

• 作为反应物：
  描述：

  甲醇 、 1,6-anhydro-N-acetylmuramic acid 在 溶剂黄146 作用下， 反应 10.0h， 生成 2-Acetamido-1,6-anhydro-2-desoxy-3-O-<(1R)-1-(methoxycarbonyl)ethyl>-β-D-glucopyranose
  参考文献：
  名称：

  Bacterial AmpD at the Crossroads of Peptidoglycan Recycling and Manifestation of Antibiotic Resistance

  摘要：

  The bacterial, enzyme AmpD is an early catalyst in commitment of cell wall metabolites to the recycling events within the cytoplasm. The key internalized metabolite of Cell watt recycling, beta-D-N-acetytgtucosamine-(1 -> 4)-1,6-anhydro-beta-N-acetytmuramyl-L-Ala-gamma-D-Glu-meso-DAP-D-Ala-D-Ala (compound 1), is a poor substrate for AmpD. Two additional metabolites, 1,6-anhydro-N-acetyimuramyl-peptidyl derivatives 2a and 2c, served as substrates for AmpD with a k(cat)/K-m of >10(4) M-1 s(-1). The enzyme hydrolytically processes the lactyl amide bond of the 1,6-anhydro-N-acetylmuramyl moiety. The syntheses of these substrates and other ligands are reported herein, which made the characterization of the enzymic reaction possible. Furthermore, it is documented that the enzyme is specific for both the atypical peptide stem of the cell wall fragments and the presence of the sterically encumbered 1,6-anhydro-N-acetylmuramyl moiety; hence it is a peptidase with a unique function in bacterial. physiology. The implications of the function of this catalyst for the entry into the cell wall recycling events and the reversal of induction of the production of beta-lactamase, an antibiotic resistance determinant, are discussed.

  DOI：

  10.1021/ja9025566
• 作为产物：
  描述：

  2-Acetamido-1,6-anhydro-4-O-benzyl-3,O-<(1R)-1-carboxyethyl>-2-desoxy-β-D-glucopyranose 在 palladium 10% on activated carbon 、 氢气 作用下， 生成 1,6-anhydro-N-acetylmuramic acid
  参考文献：
  名称：

  Bacterial AmpD at the Crossroads of Peptidoglycan Recycling and Manifestation of Antibiotic Resistance

  摘要：

  The bacterial, enzyme AmpD is an early catalyst in commitment of cell wall metabolites to the recycling events within the cytoplasm. The key internalized metabolite of Cell watt recycling, beta-D-N-acetytgtucosamine-(1 -> 4)-1,6-anhydro-beta-N-acetytmuramyl-L-Ala-gamma-D-Glu-meso-DAP-D-Ala-D-Ala (compound 1), is a poor substrate for AmpD. Two additional metabolites, 1,6-anhydro-N-acetyimuramyl-peptidyl derivatives 2a and 2c, served as substrates for AmpD with a k(cat)/K-m of >10(4) M-1 s(-1). The enzyme hydrolytically processes the lactyl amide bond of the 1,6-anhydro-N-acetylmuramyl moiety. The syntheses of these substrates and other ligands are reported herein, which made the characterization of the enzymic reaction possible. Furthermore, it is documented that the enzyme is specific for both the atypical peptide stem of the cell wall fragments and the presence of the sterically encumbered 1,6-anhydro-N-acetylmuramyl moiety; hence it is a peptidase with a unique function in bacterial. physiology. The implications of the function of this catalyst for the entry into the cell wall recycling events and the reversal of induction of the production of beta-lactamase, an antibiotic resistance determinant, are discussed.

  DOI：

  10.1021/ja9025566

文献信息

• An efficient synthesis of 1,6-anhydro-<i>N</i>-acetylmuramic acid from <i>N</i>-acetylglucosamine
  作者：Matthew B Calvert、Christoph Mayer、Alexander Titz

  DOI：10.3762/bjoc.13.261

  日期：——

  A novel synthesis of 1,6-anhydro-N-acetylmuramic acid is described, which proceeds in only five steps from the cheap starting material N-acetylglucosamine. This efficient synthesis should enable future studies into the importance of 1,6-anhydromuramic acid in bacterial cell wall recycling processes.

  描述了一种新颖的1，6-脱水-N-乙酰基尿酸的合成，其从廉价的起始原料N-乙酰基葡糖胺仅需五个步骤进行。这种有效的合成方法应该使将来的研究成为细菌细胞壁回收过程中1，6-脱水尿酸的重要性。
• Bausteine von Oligosacchariden, LXIX. Synthese von 1,6-Anhydromuramylpeptiden
  作者：Hans Paulsen、Peter Himpkamp、Thomas Peters

  DOI：10.1002/jlac.198619860408

  日期：1986.4.15

  effektive Synthese für die 1,6-Anhydro-β-muraminsäure 8 angegeben. Die Kupplung zum Disaccharid 13 mit 3,4,6-Tri-O-acetyl-2-desoxy-2-phthalimido-β-D-glucopyranosylbromid (12) als Glycosyldonator gelingt in sehr guter Ausbeute mit Silbertriflat und aktiviertem Molekularsieb (10 Å). Die Peptidkupplung des Disaccharides 15 mit dem Dipeptid 9 führt zu 16, aus dem das 1,6-Anhydromuramylpeptid β-D-GlcNAc-(1 4)-1

  给出了1，6-脱水-β-山梨酸8的有效合成。通过三氟甲磺酸银和活化的分子，与作为糖基供体的3,4,6-三-O-乙酰基-2-脱氧-2-邻苯二甲酰亚胺-β-D-吡喃葡萄糖基溴化物（12）偶联至二糖13的收率非常好筛（10Å）。二糖15与二肽9的肽偶联导致16，从中得到1,6-脱水村酰胺基肽β-D-GlcNAc-（1 4）-1,6-脱水-β-MurNAc-L-Ala-D可以得到-异-GlnOH（17）。
• WO2020109792A5
  申请人：——

  公开号：WO2020109792A5

  公开（公告）日：2022-11-09
• Synthesis of Muramyl Peptides Containing meso-Diaminopimelic Acid
  作者：Niels Kubasch、Richard R. Schmidt

  DOI：10.1002/1099-0690(200208)2002:16<2710::aid-ejoc2710>3.0.co;2-8

  日期：2002.8

  Chain-extension Of L-glutamate aldehyde 3 by means of the Wittig-Homer reaction furnished the desired C-7 dicarboxylic acid derivative, which in turn, after C-C double bond hydrogenation and protecting group manipulation, afforded the 2,6-diaminopimelic acid derivatives (S,R)-9 and (S,S)-9, both with the desired orthogonal protecting group pattern. Synthesis of the muramic acid derivative 15 and attachment of an L-alanine residue furnished muramyl-L-alanine 18. The corresponding 1,6-anhydromuramic acid derivative 26 was obtained similarly. Treatment of these compounds with peptides 28-30 and with the 2,6-diaminopimelic acid containing di- and tripeptides 32a, 32b, and 35 gave the protected muramyl peptides 17, 37, 40, 42, 44, 46, and 49a and 49b, which, after deprotection, afforded the desired target molecules muramyl-L-alanine (38), muramyl-L-alanyl-D-glutamic acid (39), muramyl-L-alanyl-D-glutaminide (41), muramyl-L-alanyl-D-isoglutaminyl-L-lysine (43), muramyl-L-alanyl-D-isoglutaminyl-(2S,6R)-2,6-diaminopimelic acid (45), muramyl-L-alanylL-isoglutaminyl-(2S,6R)-2,6-dian-Anopimelinyl-D-alanine (47), 1,6-anhydromuramyl-L-alanyl-D-isoglutaminyl-(2S,6R)-2,6-diaminopimelic acid (50a), and 1,6-anhydromuramyl-L-alanyl-Disoglutaminyl-(2S,6S)-2,6-diaminiopimelic acid (50b). (C) Wiley-VCH Verlag GmbH, 69451 Weinheim, Germany, 2002.
• Reactions of the Three AmpD Enzymes of <i>Pseudomonas aeruginosa</i>
  作者：Weilie Zhang、Mijoon Lee、Dusan Hesek、Elena Lastochkin、Bill Boggess、Shahriar Mobashery

  DOI：10.1021/ja400970n

  日期：2013.4.3

  A group of Gram-negative bacteria, including the problematic pathogen Pseudomonas aeruginosa, has linked the steps in cell-wall recycling with the ability to manifest resistance to beta-lactam antibiotics. A key step at the crossroads of the two events is performed by the protease AmpD, which hydrolyzes the peptide in the metabolite that influences these events. In contrast to other organisms that harbor this elaborate system, the genomic sequences of P. aeruginosa reveal it to have three paralogous genes for this protease, designated as ampD, ampDh2, and ampDh3. The recombinant gene products were purified to homogeneity, and their functions were assessed by the use of synthetic samples of three bacterial metabolites in cell-wall recycling and of three surrogates of cell-wall peptidoglycan. The results unequivocally identify AmpD as the bona fide recycling enzyme and AmpDh2 and AmpDh3 as enzymes involved in turnover of the bacterial cell wall itself. These findings define for the first time the events mediated by these three enzymes that lead to turnover of a key cell-wall recycling metabolite as well as the cell wall itself in its maturation.